INT235629

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Context Info
Confidence 0.76
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 3
Disease Relevance 0.81
Pain Relevance 0

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

cell differentiation (NRP1) cytosol (NRP1) signal transduction (NRP1)
extracellular region (NRP1) cell adhesion (NRP1) plasma membrane (NRP1)
NRP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 4 26.88 Quite Low
Bioavailability 2 20.16 Low Low
anesthesia 3 5.00 Very Low Very Low Very Low
imagery 3 5.00 Very Low Very Low Very Low
lidocaine 2 5.00 Very Low Very Low Very Low
fibrosis 2 5.00 Very Low Very Low Very Low
adenocard 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Diabetes Mellitus 4 92.32 High High
Obesity 14 90.28 High High
Insulin Resistance 2 88.92 High High
Death 6 75.44 Quite High
Malignant Neoplastic Disease 4 60.24 Quite High
Eye Disease 2 58.64 Quite High
Adult Respiratory Distress Syndrome 56 44.32 Quite Low
Disease 15 29.20 Quite Low
INFLAMMATION 4 26.88 Quite Low
Lung Injury 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
VEGF165b fails to phosphorylate the VEGF-R2 intracellular tyrosine residues that mediate the angiogenic response (15).
Phosphorylation (phosphorylate) of VEGF165b
1) Confidence 0.76 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0.19 Pain Relevance 0
VEGF165b binds to VEGF-R2 with equal affinity to VEGF165, but it also phosphorylates VEGF-R2 but in a qualitatively unique way (15).
Phosphorylation (phosphorylates) of VEGF165b
2) Confidence 0.59 Published 2010 Journal American Journal of Physiology - Lung Cellular and Molecular Physiology Section Body Doc Link PMC2886605 Disease Relevance 0.18 Pain Relevance 0
-subunits of the transmembrane receptor, which carry protein kinase activity, autophosphorylate on specific tyrosine residues.
Phosphorylation (autophosphorylate) of transmembrane receptor
3) Confidence 0.05 Published 2008 Journal PLoS Computational Biology Section Body Doc Link PMC2424138 Disease Relevance 0.44 Pain Relevance 0

General Comments

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